Riboflavin is a component of the Na+-pumping NADH-quinone oxidoreductase from Vibrio cholerae

Blanca Barquera; Weidong Zhou; Joel E. Morgan; Robert B. Gennis

doi:10.1073/pnas.162361299

Riboflavin is a component of the Na⁺-pumping NADH-quinone oxidoreductase from Vibrio cholerae

Blanca Barquera, Weidong Zhou, Joel E. Morgan, Robert B. Gennis

Biochemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Flavins are cofactors in many electron-transfer enzymes. Typically, two types of flavins perform this role: 5′-phosphoriboflavin (FMN) and flavin-adenine dinucleotide (FAD). Both of these are riboflavin derivatives, but riboflavin itself has never been reported to be an enzyme-bound component. We now report that tightly bound riboflavin is a component of the NADH-driven sodium pump from Vibrio cholerae.

Original language	English (US)
Pages (from-to)	10322-10324
Number of pages	3
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	99
Issue number	16
DOIs	https://doi.org/10.1073/pnas.162361299
State	Published - Aug 2002

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abstract = "Flavins are cofactors in many electron-transfer enzymes. Typically, two types of flavins perform this role: 5′-phosphoriboflavin (FMN) and flavin-adenine dinucleotide (FAD). Both of these are riboflavin derivatives, but riboflavin itself has never been reported to be an enzyme-bound component. We now report that tightly bound riboflavin is a component of the NADH-driven sodium pump from Vibrio cholerae.",

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AU - Gennis, Robert B.

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AB - Flavins are cofactors in many electron-transfer enzymes. Typically, two types of flavins perform this role: 5′-phosphoriboflavin (FMN) and flavin-adenine dinucleotide (FAD). Both of these are riboflavin derivatives, but riboflavin itself has never been reported to be an enzyme-bound component. We now report that tightly bound riboflavin is a component of the NADH-driven sodium pump from Vibrio cholerae.

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